BMRB Entry 51591

Name: Single alpha helix peptide (P3-7)2
Published: 2022-11-04

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PDB ID: 8b1x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51591
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Single alpha helix peptide (P3-7)2 PubMed: 36400768

Deposition date: 2022-08-22 Original release date: 2022-11-04

Authors: Escobedo, Albert; Piccirillo, Jonathan; Aranda, Juan; Diercks, Tammo; Mateos, Borja; Garcia-Cabau, Carla; Sanchez-Navarro, Macarena; Topal, Busra; Biesaga, Mateusz; Staby, Lasse; Kragelund, Birthe; Garcia, Jesus; Millet, Oscar; Orozco, Modesto; Coles, Murray; Crehuet, Ramon; Salvatella, Xavier

Citation: Escobedo, Albert; Piccirillo, Jonathan; Aranda, Juan; Diercks, Tammo; Mateos, Borja; Garcia-Cabau, Carla; Sanchez-Navarro, Macarena; Topal, Busra; Biesaga, Mateusz; Staby, Lasse; Kragelund, Birthe; Garcia, Jesus; Millet, Oscar; Orozco, Modesto; Coles, Murray; Crehuet, Ramon; Salvatella, Xavier. "A glutamine-based single alpha-helix scaffold to target globular proteins" Nat. Commun. 13, 7073-7073 (2022).

Assembly members:
entity_1, polymer, 25 residues, Formula weight is not available

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDEST17

Entity Sequences (FASTA):
entity_1: KKPGASLAALQALQALQAAQ AAKKY

Data sets:

RDCs
assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2
heteronucl_NOEs
- heteronucl_NOEs_1
- heteronucl_NOEs_2
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
- heteronucl_T1_relaxation_2
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1
- heteronucl_T2_relaxation_2
spectral_density_values
- spectral_density_values_1

Data type	Count
13C chemical shifts	127
15N chemical shifts	52
1H chemical shifts	305
T1 relaxation values	50
T2 relaxation values	50
heteronuclear NOE values	50
residual dipolar couplings	58
spectral density values	24

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	(P3-7)2	1

Entities:

Entity 1, (P3-7)2 25 residues - Formula weight is not available

1

LYS

PRO

GLY

ALA

SER

LEU

ALA

LEU

2

GLN

ALA

LEU

GLN

ALA

LEU

GLN

ALA

GLN

3

ALA

LYS

TYR

Samples:

sample_1: (P3-7)2, [U-100% 13C; U-100% 15N], 100 uM; DSS 10 uM; sodium phosphate 20 mM

sample_2: (P3-7)2, [U-100% 15N], 100 uM; DSS 10 uM; phosphoric acid 20 mM

sample_3: (P3-7)2, [U-100% 13C; U-100% 15N], 100 uM; DSS 10 uM; phosphoric acid 20 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D CACO	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1
3D [H]C,NH HSQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D [H]CC[CA]NH TOCSY	sample_1	isotropic	sample_conditions_1
3D [H]CC[CO]NH TOCSY	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_2	isotropic	sample_conditions_1
T1/R1 relaxation	sample_2	isotropic	sample_conditions_1
T2/R2 relaxation	sample_2	isotropic	sample_conditions_1
T2/R2 relaxation	sample_2	isotropic	sample_conditions_1
1H-15N heteronoe	sample_2	isotropic	sample_conditions_1
1H-15N heteronoe	sample_2	isotropic	sample_conditions_1
2D 1H-15N BEST-TROSY	sample_3	anisotropic	sample_conditions_1
2D 1H-15N HSQC no 13C decoupling	sample_3	anisotropic	sample_conditions_1
2D 1H-15N BEST-TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC no 13C decoupling	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

TOPSPIN - collection, processing

NMRPipe - processing

qMDD - processing

MATLAB - data analysis

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE III 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts